Dynamic structural order of a low-complexity domain facilitates assembly of intermediate filaments.
cross-beta polymerization
intermediate filaments
low-complexity proteins
solid-state NMR
Journal
Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876
Informations de publication
Date de publication:
22 09 2020
22 09 2020
Historique:
pubmed:
11
9
2020
medline:
18
11
2020
entrez:
10
9
2020
Statut:
ppublish
Résumé
The coiled-coil domains of intermediate filament (IF) proteins are flanked by regions of low sequence complexity. Whereas IF coiled-coil domains assume dimeric and tetrameric conformations on their own, maturation of eight tetramers into cylindrical IFs is dependent on either "head" or "tail" domains of low sequence complexity. Here we confirm that the tail domain required for assembly of
Identifiants
pubmed: 32907935
pii: 2010000117
doi: 10.1073/pnas.2010000117
pmc: PMC7519307
doi:
Substances chimiques
Intermediate Filament Proteins
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
23510-23518Subventions
Organisme : NIGMS NIH HHS
ID : R35 GM130358
Pays : United States
Informations de copyright
Copyright © 2020 the Author(s). Published by PNAS.
Déclaration de conflit d'intérêts
The authors declare no competing interest.
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